ID   CYSI_YERE8              Reviewed;         576 AA.
AC   A1JJS3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE            Short=SIR-HP;
DE            Short=SIRHP;
DE            EC=1.8.1.2;
GN   Name=cysI; OrderedLocusNames=YE0756;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the
RT   high pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: This enzyme catalyzes the 6-electron reduction of
CC       sulfite to sulfide. This is one of several activities required for
CC       the biosynthesis of L-cysteine from sulfate (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH.
CC   -!- COFACTOR: Binds 1 siroheme per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SUBUNIT: Alpha(8)-beta(4). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; AM286415; CAL10860.1; -; Genomic_DNA.
DR   RefSeq; YP_001005100.1; -.
DR   SMR; A1JJS3; 81-571.
DR   GeneID; 4716108; -.
DR   GenomeReviews; AM286415_GR; YE0756.
DR   KEGG; yen:YE0756; -.
DR   NMPDR; fig|630.2.peg.735; -.
DR   OMA; A1JJS3; ITTTQWQ.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:HAMAP.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_01540; -; 1.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   TIGRFAMs; TIGR02041; CysI; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    576       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000068780.
FT   METAL       435    435       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       441    441       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       480    480       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       484    484       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       484    484       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   576 AA;  64160 MW;  7D09F7F350C60B62 CRC64;
     MSEKHPGPLV VTGKLSDGER MKSQSNFLRG TIAEDLNDGL TGGFNGDNFL LIRFHGMYQQ
     DDRDIRAERA EQKLEPRHAM MLRCRLPGGI ITPQQWLGID KFAADNTLYG SIRITNRQTF
     QFHGILKGNV KPAHQLLNQL GLDALATAND VNRNVLCTSN PVESVLHQEA YEWAKKISEH
     LLPRTRAYAE IWLDAEKVAT TDEEPILGAT YLPRKFKTTV VIPPQNDVDL HANDLNFVAV
     ADKGKLVGFN VLVGGGLSIA HGDKNTYPRK ASEFGYIPLQ HTLAIAEAVV TTQRDWGNRT
     DRKNAKTKYT LERVGVEVFK AEVEKRAGVS FGAIKPYQFT GRGDRIGWVK GIDKKWHLTL
     FIENGRLLDY PGRSLKTGVA EIAKIHQGDF RLTANQNLIV AGVPEKDKAR IEALAREHGL
     MDDSVSPQRE NSMACVSFPT CPLAMAEAER FLPEFVTRIE GILQQHGLPD EHIVMRVTGC
     PNGCGRALLA EMGLVGKAVG RYNLHLGGNR EGTRIPRMYR ENITEDEILA ITDQLVGRWA
     KERHTDEGFG DFVIRVGVIA PVIDSARDFY DVQEAV
//